2dh2
From Proteopedia
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|PDB= 2dh2 |SIZE=350|CAPTION= <scene name='initialview01'>2dh2</scene>, resolution 2.10Å | |PDB= 2dh2 |SIZE=350|CAPTION= <scene name='initialview01'>2dh2</scene>, resolution 2.10Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=ACT:ACETATE ION'>ACT</scene> | + | |LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= SLC3A2, MDU1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |GENE= SLC3A2, MDU1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[2dh3|2DH3]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2dh2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dh2 OCA], [http://www.ebi.ac.uk/pdbsum/2dh2 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2dh2 RCSB]</span> | ||
}} | }} | ||
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[[Category: Fort, J.]] | [[Category: Fort, J.]] | ||
[[Category: Palacin, M.]] | [[Category: Palacin, M.]] | ||
| - | [[Category: ACT]] | ||
[[Category: antiparallel beta-sheet]] | [[Category: antiparallel beta-sheet]] | ||
[[Category: c-terminal domain]] | [[Category: c-terminal domain]] | ||
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[[Category: transport protein]] | [[Category: transport protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:34:39 2008'' |
Revision as of 23:34, 30 March 2008
| |||||||
| , resolution 2.10Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Gene: | SLC3A2, MDU1 (Homo sapiens) | ||||||
| Related: | 2DH3
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure of human ED-4F2hc
Overview
4F2hc (CD98hc) is a multifunctional type II membrane glycoprotein involved in amino acid transport and cell fusion, adhesion, and transformation. The structure of the ectodomain of human 4F2hc has been solved using monoclinic (Protein Data Bank code 2DH2) and orthorhombic (Protein Data Bank code 2DH3) crystal forms at 2.1 and 2.8 A, respectively. It is composed of a (betaalpha)(8) barrel and an antiparallel beta(8) sandwich related to bacterial alpha-glycosidases, although lacking key catalytic residues and consequently catalytic activity. 2DH3 is a dimer with Zn(2+) coordination at the interface. Human 4F2hc expressed in several cell types resulted in cell surface and Cys(109) disulfide bridge-linked homodimers with major architectural features of the crystal dimer, as demonstrated by cross-linking experiments. 4F2hc has no significant hydrophobic patches at the surface. Monomer and homodimer have a polarized charged surface. The N terminus of the solved structure, including the position of Cys(109) residue located four residues apart from the transmembrane domain, is adjacent to the positive face of the ectodomain. This location of the N terminus and the Cys(109)-intervening disulfide bridge imposes space restrictions sufficient to support a model for electrostatic interaction of the 4F2hc ectodomain with membrane phospholipids. These results provide the first crystal structure of heteromeric amino acid transporters and suggest a dynamic interaction of the 4F2hc ectodomain with the plasma membrane.
About this Structure
2DH2 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
The structure of human 4F2hc ectodomain provides a model for homodimerization and electrostatic interaction with plasma membrane., Fort J, de la Ballina LR, Burghardt HE, Ferrer-Costa C, Turnay J, Ferrer-Orta C, Uson I, Zorzano A, Fernandez-Recio J, Orozco M, Lizarbe MA, Fita I, Palacin M, J Biol Chem. 2007 Oct 26;282(43):31444-52. Epub 2007 Aug 26. PMID:17724034
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